Eukaryotic organisms synthesize oligosaccharide structures or glycoconjugates, such as glycolipids or glycoproteins, that are commercially and therapeutically useful. In vitro synthesis of oligosaccharides or glycoconjugates can be carried out using recombinant eukaryotic glycosyltransferases. The most efficient method to produce many recombinant proteins is to express the protein in bacteria. However, in bacteria, many eukaryotic glycosyltransferases are expressed as insoluble proteins in bacterial inclusion bodies, and yields of active eukaryotic glycosyltransferase protein from the inclusion bodies can be very low. In addition, many eukaryotic glycosyltransferases are expressed as glycosylated proteins in their cells of origin. Therefore, it was believed that expression of the proteins in bacteria would not include native glycosylation patterns, further decreasing the expectation of expression of active eukaryotic glycosyltransferase protein. See, e.g., Breton et al., Biochimie 83:713-718 (2001). Thus, there is a need for improved methods to produce enzymatically active eukaryotic glycosyltransferases in prokaryotic organisms, such as, e.g., bacteria. The present invention solves this and other needs.